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Structure paper

TitleStructural Basis of Tryptophan Reverse N-Prenylation Catalyzed by CymD.
Journal, issue, pagesBiochemistry, Vol. 58, Page 3232-3242, Year 2019
Publish dateMay 1, 2019 (structure data deposition date)
AuthorsRoose, B.W. / Christianson, D.W.
External linksBiochemistry / PubMed:31251043
MethodsX-ray diffraction
Resolution1.33 - 1.7 Å
Structure data

PDB-6os3:
Crystal structure of native CymD prenyltransferase
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-6os5:
Crystal structure of CymD prenyltransferase complexed with L-tryptophan
Method: X-RAY DIFFRACTION / Resolution: 1.66 Å

PDB-6os6:
Crystal structure of CymD prenyltransferase complexed with L-tryptophan and DMSPP
Method: X-RAY DIFFRACTION / Resolution: 1.33 Å

Chemicals

ChemComp-B3P:
2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-TRP:
TRYPTOPHAN

ChemComp-BEZ:
BENZOIC ACID

ChemComp-DPO:
DIPHOSPHATE

ChemComp-IMD:
IMIDAZOLE

ChemComp-DST:
DIMETHYLALLYL S-THIOLODIPHOSPHATE

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry

Source
  • salinispora arenicola (strain cns-205) (bacteria)
KeywordsTRANSFERASE / prenyltransferase / tryptophan / indole / biosynthesis

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